The folding of a protein can be described by the following reaction equation where A is the unfolded chain and B is the folded structure. Under standard conditions, this reaction is accompanied by a change in the free enthalpy of , so that the folded structure is energetically more favorable. How large is the concentration ratio of substances A and B in the reaction equilibrium?
Note: The temperature is and the general gas constant is .
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The folding of protein is a first-order reaction because only one molecule is involved at a time. The reaction rates then became d t d [ A ] d t d [ B ] = − k A → B [ A ] + k B → A [ B ] = − k B → A [ B ] + k A → B [ A ] where the coefficients, k A → B and k B → A , describe the foward and backward reaction, respectively. In equilibrium, the net reaction rates are zero, so that d t d [ A ] = d t d [ B ] = 0 ⇒ [ A ] [ B ] = k B → A k A → B The coefficients follow Arhenius law k A → B k B → A = C exp ( − R T Δ G A ) = C exp ( − R T Δ G A − Δ G ) where Δ G A is the activation free enthalpy and Δ G < 0 is the reaction free enthalpy.
Finally, the concentration ratio results to [ A ] [ B ] = k B → A k A → B = exp ( − R T Δ G ) = exp ( 8 . 3 1 4 ⋅ 2 9 8 2 3 0 0 0 ) ≈ 1 . 0 8 ⋅ 1 0 4